Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.320 extracted from

  • Zhu, J.; Zhang, D.; Liu, X.; Yu, G.; Cai, X.; Xu, C.; Rong, F.; Ouyang, G.; Wang, J.; Xiao, W.
    Zebrafish prmt5 arginine methyltransferase is essential for germ cell development (2019), Development, 146, dev179572 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 S-adenosyl-L-methionine + [germ cell-specific protein Vasa]-L-arginine Danio rerio seven arginine residues in Vasa, including R101, R105, R177, R179, R183, R197 and R201, and two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Vasa mutant with seven arginines to lysines (Vasa-7M: R101K, R105K, R177K, R179K, R183K, R197K and R201K) can not be dimethylated by Prmt5 2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine Danio rerio two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Zili mutant with two arginines to lysines [Zili (1-133aa)-R68/221K] can not be dimethylated by Prmt5 2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
-
?
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine Danio rerio
-
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine Danio rerio
-
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
-
?

Organism

Organism UniProt Comment Textmining
Danio rerio B0R026
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + [germ cell-specific protein Vasa]-L-arginine
-
Danio rerio 2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Vasa]-L-arginine seven arginine residues in Vasa, including R101, R105, R177, R179, R183, R197 and R201, and two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Vasa mutant with seven arginines to lysines (Vasa-7M: R101K, R105K, R177K, R179K, R183K, R197K and R201K) can not be dimethylated by Prmt5 Danio rerio 2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine
-
Danio rerio 2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Zili mutant with two arginines to lysines [Zili (1-133aa)-R68/221K] can not be dimethylated by Prmt5 Danio rerio 2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
-
?
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
-
Danio rerio 2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
-
Danio rerio 2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
-
?

Synonyms

Synonyms Comment Organism
PRMT5
-
Danio rerio
protein arginine methyltransferase 5
-
Danio rerio

General Information

General Information Comment Organism
malfunction prmt5 loss in zebrafish leads to the expression of an infertile male phenotype due to a reduction in germ cell number, an increase in germ cell apoptosis and the failure of gonads to differentiate into normal testes or ovaries. Arginine methylation of the germ cell-specific proteins Zili and Vasa, as well as histones H3 (H3R8me2s) and H4 (H4R3me2s), is reduced in the gonads of prmt5-null zebrafish Danio rerio
physiological function protein arginine methyltransferase 5 (Prmt5) symmetrically dimethylates arginine in nuclear and cytoplasmic proteins. Prmt5 is involved in a variety of cellular processes, including ribosome biogenesis, cellular differentiation, germ cell development and tumorigenesis Danio rerio